Structure of Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Site 412 to 423 in Complex with Antibody AP33 |
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| Authors: | Leopold Kong Erick Giang Travis Nieusma Justin B. Robbins Marc C. Deller Robyn L. Stanfield Ian A. Wilson Mansun Law |
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| Affiliation: | aDepartments of Molecular Biology;bImmunology and Microbial Science;cThe Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA;dJoint Center for Structural Genomics, La Jolla, California, USA |
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| Abstract: | We have determined the crystal structure of the broadly neutralizing antibody (bnAb) AP33, bound to a peptide corresponding to hepatitis C virus (HCV) E2 envelope glycoprotein antigenic site 412 to 423. Comparison with bnAb HCV1 bound to the same epitope reveals a different angle of approach to the antigen by bnAb AP33 and slight variation in its β-hairpin conformation of the epitope. These structures establish two different modes of binding to E2 that antibodies adopt to neutralize diverse HCV. |
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